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Database: UniProt
Entry: A0A139TRK2_9BACT
LinkDB: A0A139TRK2_9BACT
Original site: A0A139TRK2_9BACT 
ID   A0A139TRK2_9BACT        Unreviewed;      1050 AA.
AC   A0A139TRK2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=HMPREF3039_01557 {ECO:0000313|EMBL:KXU54229.1};
OS   Akkermansia sp. KLE1798.
OC   Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC   Akkermansiaceae; Akkermansia.
OX   NCBI_TaxID=1574265 {ECO:0000313|EMBL:KXU54229.1, ECO:0000313|Proteomes:UP000070454};
RN   [1] {ECO:0000313|EMBL:KXU54229.1, ECO:0000313|Proteomes:UP000070454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1798 {ECO:0000313|EMBL:KXU54229.1,
RC   ECO:0000313|Proteomes:UP000070454};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXU54229.1}.
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DR   EMBL; LTZM01000033; KXU54229.1; -; Genomic_DNA.
DR   RefSeq; WP_067571544.1; NZ_KQ971081.1.
DR   AlphaFoldDB; A0A139TRK2; -.
DR   PATRIC; fig|1574265.3.peg.1514; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000070454; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          1..467
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          468..717
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1050 AA;  118604 MW;  18A43D9CBCB4C8EC CRC64;
     MSALTNILIS ASAGTGKTYQ LSLRFLALLV LNRGSHPERL IAVTFTRKAA GEFKDRILTD
     LAAGATDSAG AARLRDRLWA VIKGTPEEPG LWPQAAESWK KEHLCQERFR HMLRLLVQQL
     SRLNLCTIDS LFAQIAATST FELGVSGFSM IDTTAEKLAR REALLTLYRE CSLNPEQEQS
     FEDAFLSGAD SDAEAADAED SMARRLNTYH ELFLDESDTG KWGNPATLGF TPEELLPPVP
     LERFNAALHA LMDRARDMPA PEGRNGAKNK EMFLRFLNGF STYVKLGRLK FHDTEKKLTM
     EEAREKFRDF WSPPLDELIQ SWLRMETLQA LHRTRSTHGL MRIFEDKYSA LVRNKGRFLF
     HDVTRMLGNG AVTPELKRDL QYRMYCRYDH WMLDEFQDTS QSQWRVIKPF LDDLTDTREE
     QEGSIFVVGD LKQSVYQWRG GDPALFRSVA GQLHLEERGM ATSYRSVQPV LDMVNDICDY
     ARTAADCGQA ALEQWGDYPP HVCAPSLASR TGCARIWQTP RAEETSANDL VCQAMADILE
     QSNALRRGLD VAVLVSTRNQ ALIVREWLTS HGWPAEVCDD VPVGQDSPLG KTLLSFFRWL
     LSPGDAFISG LLSHSPLHPL ISPDRRPGMD WNGWHMVLER EGYAAIMTEL EKRMALAGVE
     LTDFHRDRLS VWMNEAEQVD ERGASLDEWI RRMEDLTRRE DPSGGIVRIM TIHKSKGLGF
     DMVILPQIGK DAPFADSRHL THFVKRDGNG LVEGIVMAPS KQVYTAVPQF HALYESWKAT
     QQFDGFCKLY VALTRARRAC HIILPGREGK GELRTESMWK IIRSAALAAS CGTEDTLPES
     GAECLYSRGE PEWYAELPEK DTRTEPENAP EWPVHKPLLR QRVSPSGLDG ENGLFRSMHD
     AALRESAAFG SAVHAVFERI TRWNGEDKPH WVLHPVTEAE RTVAACMDVP AIRELFMPAE
     TAIVMKEQRI EAIDGNVWIS GVIDRLVIDG DSACIVDFKT DHADTAEQLR ERHGAQLQAY
     ARIVSKITRI PCDRIRRMII STHLKTVIQV
//
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